ArticleThe Journal of biological chemistry2011
Structural plasticity of the thioredoxin recognition site of yeast methionine S-sulfoxide reductase Mxr1.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 28 citations in OpenAlex.
- Dietary drivers of gut microbiota diversity and function in wildlife of Wolong Nature Reserve: a metagenomic study.Current zoology · 2026Article
- Discovery and Rational Mutagenesis of Methionine Sulfoxide Reductase Biocatalysts To Expand the Substrate Scope of the Kinetic Resolution of Chiral Sulfoxides.ACS catalysis · 2023Article
- Article
- Intra- and inter-protein couplings of backbone motions underlie protein thiol-disulfide exchange cascade.Scientific reports · 2018Article
- Monitoring thioredoxin redox with a genetically encoded red fluorescent biosensor.Nature chemical biology · 2017Article
- Practical guide for dynamic monitoring of protein oxidation using genetically encoded ratiometric fluorescent biosensors of methionine sulfoxide.Methods (San Diego, Calif.) · 2016Review
- The specificity of thioredoxins and glutaredoxins is determined by electrostatic and geometric complementarity.Chemical science · 2015Article
- A universal entropy-driven mechanism for thioredoxin-target recognition.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Monitoring methionine sulfoxide with stereospecific mechanism-based fluorescent sensors.Nature chemical biology · 2015Article
- Structural snapshots of yeast alkyl hydroperoxide reductase Ahp1 peroxiredoxin reveal a novel two-cysteine mechanism of electron transfer to eliminate reactive oxygen species.The Journal of biological chemistry · 2012Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The methionine S-sulfoxide reductase MsrA catalyzes the reduction of methionine sulfoxide, a ubiquitous reaction depending on the thioredoxin system. To investigate interactions between MsrA and thioredoxin (Trx), we determined the crystal structures of yeast MsrA/Mxr1 in their reduced, oxidized, and Trx2-complexed forms, at 2.03, 1.90, and 2.70 Å, respectively. Comparative structure analysis revealed significant conformational changes of the three loops, which form a plastic "cushion" to harbor the electron donor Trx2. The flexible C-terminal loop enabled Mxr1 to access the methionine sulfoxide on various protein substrates. Moreover, the plasticity of the Trx binding site on Mxr1 provides structural insights into the recognition of diverse substrates by a universal catalytic motif of Trx.
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